| Literature DB >> 17306216 |
Joanne M Santini1, Ulrike Kappler, Seamus A Ward, Michael J Honeychurch, Rachel N vanden Hoven, Paul V Bernhardt.
Abstract
Arsenite oxidation by the facultative chemolithoautotroph NT-26 involves a periplasmic arsenite oxidase. This enzyme is the first component of an electron transport chain which leads to reduction of oxygen to water and the generation of ATP. Involved in this pathway is a periplasmic c-type cytochrome that can act as an electron acceptor to the arsenite oxidase. We identified the gene that encodes this protein downstream of the arsenite oxidase genes (aroBA). This protein, a cytochrome c(552), is similar to a number of c-type cytochromes from the alpha-Proteobacteria and mitochondria. It was therefore not surprising that horse heart cytochrome c could also serve, in vitro, as an alternative electron acceptor for the arsenite oxidase. Purification and characterisation of the c(552) revealed the presence of a single heme per protein and that the heme redox potential is similar to that of mitochondrial c-type cytochromes. Expression studies revealed that synthesis of the cytochrome c gene was not dependent on arsenite as was found to be the case for expression of aroBA.Entities:
Mesh：
Substances：
Year: 2007 PMID： 17306216 DOI： 10.1016/j.bbabio.2007.01.009
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002